8S1M
Crystal structure of human GABARAP fused to EGFR (1076-1099)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-3 |
Synchrotron site | ESRF |
Beamline | MASSIF-3 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-09-17 |
Detector | DECTRIS EIGER X 4M |
Wavelength(s) | 0.9677 |
Spacegroup name | I 2 3 |
Unit cell lengths | 101.280, 101.280, 101.280 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 41.350 - 2.050 |
R-factor | 0.2055 |
Rwork | 0.203 |
R-free | 0.22980 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.595 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 41.350 | 2.100 |
High resolution limit [Å] | 2.050 | 2.050 |
Number of reflections | 11007 | 798 |
<I/σ(I)> | 21.91 | 1.01 |
Completeness [%] | 100.0 | 99.1 |
Redundancy | 20.1 | 20.1 |
CC(1/2) | 1.000 | 0.365 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 293 | 0.17 M ammonium acetate 0.085 M sodium citrate 25.5% PEG 4000 15% Glycerol |